Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions (Q24320262)

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24 February 2020

title

Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions (English)

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24 February 2020

1

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24 February 2020

Pascal Schneider

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24 February 2020

author name string

Laure Willen

2

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24 February 2020

Mai Perroud

3

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24 February 2020

Dennis Krushinskie

4

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24 February 2020

Kathy Strauch

5

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24 February 2020

Hernan Cuervo

6

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24 February 2020

Eric S Day

7

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24 February 2020

Timothy S Zheng

9

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24 February 2020

language of work or name

English

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publication date

18 March 2013

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24 February 2020

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24 February 2020

volume

280

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24 February 2020

issue

8

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page(s)

1818-1829

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The TNF and TNF receptor superfamilies: integrating mammalian biology

24 February 2020

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Molecular structure and characterization of the cytokine TWEAK and its receptor Fn14 in bovine.

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Molecular characterization of the canine cytokine TWEAK (CD255) and its receptor, Fn14 (CD266).

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Molecular characterization of cytokine TWEAK and its receptor Fn14 in pig (Sus scrofa).

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TWEAKing tissue remodeling by a multifunctional cytokine: role of TWEAK/Fn14 pathway in health and disease

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TWEAK/Fn14 pathway: an immunological switch for shaping tissue responses

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Therapeutic targeting of TWEAK/Fnl4 in cancer: exploiting the intrinsic tumor cell killing capacity of the pathway

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BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site

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Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding

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Crystal structure of the BAFF–BAFF-R complex and its implications for receptor activation

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TWEAK binding to the Fn14 cysteine-rich domain depends on charged residues located in both the A1 and D2 modules

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Studies of binding of tumor necrosis factor (TNF)-like weak inducer of apoptosis (TWEAK) to fibroblast growth factor inducible 14 (Fn14).

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Selectivity of BAFF/BLyS and APRIL for binding to the TNF family receptors BAFFR/BR3 and BCMA.

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Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily

21 January 2018

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Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation

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Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity

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Widespread parallel evolution in sticklebacks by repeated fixation of Ectodysplasin alleles

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Wengen, a member of the Drosophila tumor necrosis factor receptor superfamily, is required for Eiger signaling

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Formation of virus-like clusters is an intrinsic property of the tumor necrosis factor family member BAFF (B cell activating factor).

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inferred from DOI database lookup

7 January 2021

based on heuristic

Production of recombinant TRAIL and TRAIL receptor: Fc chimeric proteins

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inferred from DOI database lookup

7 January 2021

based on heuristic

Unique and conserved functions of B cell-activating factor of the TNF family (BAFF) in the chicken

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1111/FEBS.12206

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23438059%20AND%20SRC:MED&resulttype=core&format=json

24 February 2020

1 reference